Antimalarial drug discovery: targeting protein kinases

Bibliography

• SACHS J, MALANEY P: The economic and social burden of malaria. Nature (2002) 415(6872):680-685.
   PubMed Web of Science ®Google Scholar
• BREMAN JG, ALILIO MS, MILLS A: Conquering the intolerable burden of malaria: what’s new, what’s needed: a summary. Am. J. Trop. Med. Hyg. (2004) 71(2 Suppl.):1-15.
   PubMed Web of Science ®Google Scholar
• GREENWOOD B, MUTABINGWA T: Malaria in 2002. Nature (2002) 415(6872):670-672.
   PubMed Web of Science ®Google Scholar
• RIDLEY RG: Medical need, scientific opportunity and the drive for antimalarial drugs. Nature (2002) 415:686-693.
   PubMed Web of Science ®Google Scholar
• RIDLEY RG: Introduction. Antimalarial drug resistance: ramifications, explanations and challenges. Microbes Infect. (2002) 4(2):155-156.
   PubMedGoogle Scholar
• TROUILLER P, OLLIARO P, TORREELE E et al.: Drug development for neglected diseases: a deficient market and a public-health policy failure. Lancet (2002) 359(9324):2188-2194.
   PubMed Web of Science ®Google Scholar
• KOSTICH M, ENGLISH J, MADISON V et al.: Human members of the eukaryotic protein kinase family. Genome Biol. (2002) 3(9):Research 0043.0041-0043.0012.
   Google Scholar
• MANNING G, WHYTE DB, MARTINEZ R, HUNTER T, SUDARSANAM S: The protein kinase complement of the human genome. Science (2002) 298(5600):1912-1934.
   PubMed Web of Science ®Google Scholar
• NIEDNER RH, BUZKO OV, HASTE NM et al.: Protein kinase resource: an integrated environment for phosphorylation research. Proteins (2006) 63(1):78-86.
   PubMed Web of Science ®Google Scholar
• COHEN P: Protein kinases-the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. (2002) 1(4):309-315.
   PubMed Web of Science ®Google Scholar
• FISCHER PM: The design of drug candidate molecules as selective inhibitors of therapeutically relevant protein kinases. Curr. Med. Chem. (2004) 11(12):1563-1583.
   PubMed Web of Science ®Google Scholar
• WEINMANN H, METTERNICH R: Drug discovery process for kinase inhibitors. Chembiochem (2005) 6(3):455-459.
   PubMed Web of Science ®Google Scholar
• BALDAUF SL: The deep roots of eukaryotes. Science (2003) 300(5626):1703-1706.
   PubMed Web of Science ®Google Scholar
• KAPPES B, DOERIG CD, GRAESER R: An overview of Plasmodium protein kinases. Parasitol. Today (1999) 15(11):449-454.
   PubMedGoogle Scholar
• ANAMIKA, SRINIVASAN N, KRUPA A: A genomic perspective of protein kinases in Plasmodium falciparum. Proteins (2005) 58(1):180-189.
   PubMed Web of Science ®Google Scholar
• WARD P, EQUINET L, PACKER J, DOERIG C: Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics (2004) 5(1):79.
   PubMed Web of Science ®Google Scholar
• DOERIG C: Protein kinases as targets for anti-parasitic chemotherapy. Biochim. Biophys. Acta (2004) 1697:155-168.
   PubMed Web of Science ®Google Scholar
• DOERIG C, BILLKER O, PRATT D, ENDICOTT J: Protein kinases as targets for antimalarial intervention: kinomics, structure-based design, transmission-blockade, and targeting host cell enzymes. Biochim. Biophys. Acta (2005) 1754(1-2):132-150.
   PubMed Web of Science ®Google Scholar
• HARTWELL LH: Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J. Cell Biol. (1980) 85(3):811-822.
   PubMed Web of Science ®Google Scholar
• SCHNEIDER AG, MERCEREAU-PUIJALON O: A new Apicomplexa-specific protein kinase family: multiple members in Plasmodium falciparum, all with an export signature. BMC Genomics (2005) 6(1):30.
   PubMed Web of Science ®Google Scholar
• NUNES M, GOLDRING P, DOERIG C, SCHERF A: A novel protein kinase family in Plasmodium falciparum is differentially transcribed and secreted to different cellular compartments of the host cell. Mol. Microbiol. (2007) 63:391-403.
   PubMedGoogle Scholar
• PARSONS M, WORTHEY EA, WARD PN, MOTTRAM JC: Comparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. BMC Genomics (2005) 6:127.
   PubMed Web of Science ®Google Scholar
• CHENG SH, WILLMANN MR, CHEN HC, SHEEN J: Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family. Plant Physiol. (2002) 129(2):469-485.
   PubMed Web of Science ®Google Scholar
• DOERIG CM, PARZY D, LANGSLEY G et al.: A MAP kinase homologue from the human malaria parasite, Plasmodium falciparum. Gene (1996) 177(1-2):1-6.
   PubMedGoogle Scholar
• DORIN D, ALANO P, BOCCACCIO I et al.: An atypical mitogen-activated protein kinase (MAPK) homologue expressed in gametocytes of the human malaria parasite Plasmodium falciparum. Identification of a MAPK signature. J. Biol. Chem. (1999) 274(42):29912-29920.
   PubMedGoogle Scholar
• DORIN D, SEMBLAT JP, POULLET P et al.: PfPK7, an atypical MEK-related protein kinase, reflects the absence of typical three-component MAP kinase pathways in the human malaria parasite Plasmodium falciparum. Mol. Microbiol. (2005) 55(1):184-196.
   PubMed Web of Science ®Google Scholar
• LIN DT, GOLDMAN ND, SYIN C: Stage-specific expression of a Plasmodium falciparum protein related to the eukaryotic mitogen-activated protein kinases. Mol. Biochem. Parasitol. (1996) 78(1-2):67-77.
   PubMedGoogle Scholar
• DENG W, PARBHU-PATEL A, MEYER DJ, BAKER DA: The role of two novel regulatory sites in the activation of the cGMP-dependent protein kinase from Plasmodium falciparum. Biochem. J. (2003) 374(Pt. 2):559-565.
   PubMedGoogle Scholar
• DORIN D, LE ROCH K, SALLICANDRO P et al.: Pfnek-1, a NIMA-related kinase from the human malaria parasite Plasmodium falciparum. Biochemical properties and possible involvement in MAPK regulation. Eur. J. Biochem. (2001) 268(9):2600-2608.
   PubMedGoogle Scholar
• BRACCHI-RICARD V, BARIK S, DELVECCHIO C et al.: PfPK6, a novel cyclin-dependent kinase/mitogen-activated protein kinase- related protein kinase from Plasmodium falciparum. Biochem. J. (2000) 347(Pt. 1):255-263.
   PubMedGoogle Scholar
• MENARD R, JANSE C: Gene targeting in malaria parasites. Methods (1997) 13(2):148-157.
   PubMed Web of Science ®Google Scholar
• LI JL, ROBSON KJ, CHEN JL, TARGETT GA, BAKER DA: Pfmrk, a MO15-related protein kinase from Plasmodium falciparum. Gene cloning, sequence, stage-specific expression and chromosome localization. Eur. J. Biochem. (1996) 241(3):805-813.
   PubMedGoogle Scholar
• XIAO Z, WATERS NC, WOODARD CL, LI Z, LI PK: Design and synthesis of Pfmrk inhibitors as potential antimalarial agents. Bioorg. Med. Chem. Lett (2001) 11(21):2875-2878.
   PubMed Web of Science ®Google Scholar
• GEYER JA, PRIGGE ST, WATERS NC: Targeting malaria with specific CDK inhibitors. Biochim. Biophys. Acta (2005) 1754(1-2):160-170.
   PubMedGoogle Scholar
• KEENAN SM, GEYER JA, WELSH WJ, PRIGGE ST, WATERS NC: Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors. Comb. Chem. High Throughput Screen. (2005) 8(1):27-38.
   PubMed Web of Science ®Google Scholar
• LAURENT D, JULLIAN V, PARENTY A et al.: Antimalarial potential of xestoquinone, a protein kinase inhibitor isolated from a Vanuatu marine sponge Xestospongia sp. Bioorg. Med. Chem. (2006) 14(13):4477-4482.
   PubMed Web of Science ®Google Scholar
• RANGARAJAN R, BEI AK, JETHWANEY D et al.: A mitogen-activated protein kinase regulates male gametogenesis and transmission of the malaria parasite Plasmodium berghei. EMBO Rep. (2005) 6(5):464-469.
   PubMed Web of Science ®Google Scholar
• TEWARI R, DORIN D, MOON R, DOERIG C, BILLKER O: An atypical mitogen-activated protein kinase controls cytokinesis and flagellar motility during male gamete formation in a malaria parasite. Mol. Microbiol. (2005) 58(5):1253-1263.
   PubMed Web of Science ®Google Scholar
• ZHAO Y, POKUTTA S, MAURER P et al.: Calcium-binding properties of a calcium-dependent protein kinase from Plasmodium falciparum and the significance of individual calcium- binding sites for kinase activation. Biochemistry (1994) 33(12):3714-3721.
   PubMedGoogle Scholar
• FARBER PM, GRAESER R, FRANKLIN RM, KAPPES B: Molecular cloning and characterization of a second calcium-dependent protein kinase of Plasmodium falciparum. Mol. Biochem. Parasitol. (1997) 87(2):211-216.
   PubMedGoogle Scholar
• LI JL, BAKER DA, COX LS: Sexual stage-specific expression of a third calcium-dependent protein kinase from Plasmodium falciparum. Biochim. Biophys. Acta (2000) 1491(1-3):341-349.
   PubMedGoogle Scholar
• DROUCHEAU E, PRIMOT A, THOMAS V et al.: Plasmodium falciparum glycogen synthase kinase-3: molecular model, expression, intracellular localisation and selective inhibitors. Biochim. Biophys. Acta (2004) 1697(1-2):181-196.
   PubMed Web of Science ®Google Scholar
• ROSS-MACDONALD PB, GRAESER R, KAPPES B, FRANKLIN R, WILLIAMSON DH: Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite Plasmodium falciparum. Eur. J. Biochem. (1994) 220(3):693-701.
   PubMedGoogle Scholar
• DOERIG C, ENDICOTT J, CHAKRABARTI D: Cyclin-dependent kinase homologues of Plasmodium falciparum. Int. J. Parasitol. (2002) 32(13):1575-1585.
   PubMed Web of Science ®Google Scholar
• KUMAR A, VAID A, SYIN C, SHARMA P: PfPKB, a novel protein kinase B like enzyme from Plasmodium falciparum: I. Identification, characterization and possible role in parasite development. J. Biol. Chem. (2004) 279(23):24255-24264.
   PubMedGoogle Scholar
• SYIN C, PARZY D, TRAINCARD F et al.: The H89 cAMP-dependent protein kinase inhibitor blocks Plasmodium falciparum development in infected erythrocytes. Eur. J. Biochem. (2001) 268(18):4842-4849.
   PubMedGoogle Scholar
• VAID A, SHARMA P: PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum: II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway. J. Biol. Chem. (2006) 281(37):27126-27133.
   PubMedGoogle Scholar
• GRAY NS, WODICKA L, THUNNISSEN AM et al.: Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors. Science (1998) 281(5376):533-538.
   PubMed Web of Science ®Google Scholar
• SINDEN RE, BUTCHER GA, BILLKER O, FLECK SL: Regulation of infectivity of Plasmodium to the mosquito vector. Adv. Parasitol. (1996) 38:53-117.
   PubMedGoogle Scholar
• LOOAREESUWAN S, CHULAY JD, CANFIELD CJ, HUTCHINSON DB: Malarone (atovaquone and proguanil hydrochloride): a review of its clinical development for treatment of malaria. Malarone Clinical Trials Study Group. Am. J. Trop. Med. Hyg. (1999) 60(4):533-541.
   PubMed Web of Science ®Google Scholar
• VAIDYA AB, MATHER MW: Atovaquone resistance in malaria parasites. Drug Resist. Updat. (2000) 3(5):283-287.
   PubMedGoogle Scholar
• NIVEZ M, ACHBAROU A, BIENVENU JD et al.: A study of selected Plasmodium yoelii messenger RNAs during hepatocyte infection. Mol. Biochem. Parasitol. (2000) 111(1):31-39.
   PubMedGoogle Scholar
• WATERS AP, JANSE CJ: The development of and perspectives for genetic engineering of malaria parasites. Parassitologia (1999) 41(1-3):453-459.
   PubMedGoogle Scholar
• CARVALHO TG, MENARD R: Manipulating the Plasmodium genome. Curr. Issues Mol. Biol. (2005) 7(1):39-55.
   PubMed Web of Science ®Google Scholar
• BISHOP AC, BUZKO O, SHOKAT KM: Magic bullets for protein kinases. Trends Cell Biol. (2001) 11(4):167-172.
   PubMed Web of Science ®Google Scholar
• BILLKER O, DECHAMPS S, TEWARI R et al.: Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite. Cell (2004) 117(4):503-514.
   PubMed Web of Science ®Google Scholar
• KHAN SM, FRANKE-FAYARD B, MAIR GR et al.: Proteome analysis of separated male and female gametocytes reveals novel sex-specific Plasmodium biology. Cell (2005) 121(5):675-687.
   PubMed Web of Science ®Google Scholar
• REININGER L, BILLKER O, TEWARI R et al.: A nima-related protein kinase is essential for completion of the sexual cycle of malaria parasites. J. Biol. Chem. (2005) 280(36):31957-31964.
   PubMed Web of Science ®Google Scholar
• ISHINO T, ORITO Y, CHINZEI Y, YUDA M: A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell. Mol. Microbiol. (2006) 59(4):1175-1184.
   PubMedGoogle Scholar
• SIDEN-KIAMOS I, ECKER A, NYBACK S, LOUIS C, SINDEN RE, BILLKER O: Plasmodium berghei calcium-dependent protein kinase 3 is required for ookinete gliding motility and mosquito midgut invasion. Mol. Microbiol. (2006) 60(6):1355-1363.
   PubMed Web of Science ®Google Scholar
• DOERIG C, MEIJER L, MOTTRAM JC: Protein kinases as drug targets in parasitic protozoa. Trends Parasitol. (2002) 18(8):366-371.
   PubMed Web of Science ®Google Scholar
• DAUB H, GODL K, BREHMER D, KLEBL B, MULLER G: Evaluation of kinase inhibitor selectivity by chemical proteomics. Assay Drug Dev. Technol. (2004) 2(2):215-224.
   PubMedGoogle Scholar
• VALSASINA B, KALISZ HM, ISACCHI A: Kinase selectivity profiling by inhibitor affinity chromatography. Expert Rev. Proteomics (2004) 1(3):303-315.
   PubMed Web of Science ®Google Scholar
• BACH S, BLONDEL M, MEIJER L: Evaluation of CDK inhibitors’ selectivity: from affinity chromatography to yeast genetics. Yue E et al. (Eds.) CRC Press, Taylor & Francis, UK (2006):103-119.
   Google Scholar
• HAYSTEAD TA: The purinome, a complex mix of drug and toxicity targets. Curr. Top. Med. Chem. (2006) 6(11):1117-1127.
   PubMedGoogle Scholar
• BACH S, KNOCKAERT M, REINHARDT J et al.: Roscovitine targets, protein kinases and pyridoxal kinase. J. Biol. Chem. (2005) 280(35):31208-31219.
   PubMed Web of Science ®Google Scholar
• HARMSE L, VAN ZYL R, GRAY N et al.: Structure-activity relationships and inhibitory effects of various purine derivatives on the in vitro growth of Plasmodium falciparum. Biochem. Pharmacol. (2001) 62(3):341-348.
   PubMed Web of Science ®Google Scholar
• KNOCKAERT M, GRAY N, DAMIENS E et al.: Intracellular targets of cyclin-dependent kinase inhibitors: identification by affinity chromatography using immobilised inhibitors. Chem. Biol. (2000) 7(6):411-422.
   PubMed Web of Science ®Google Scholar
• GURNETT AM, LIBERATOR PA, DULSKI PM et al.: Purification and molecular characterization of cGMP-dependent protein kinase from Apicomplexan parasites. A novel chemotherapeutic target. J. Biol. Chem. (2002) 277(18):15913-15922.
   PubMed Web of Science ®Google Scholar
• WIERSMA HI, GALUSKA SE, TOMLEY FM et al.: A role for coccidian cGMP-dependent protein kinase in motility and invasion. Int. J. Parasitol. (2004) 34(3):369-380.
   PubMed Web of Science ®Google Scholar
• DONALD RG, ALLOCCO J, SINGH SB et al.: Toxoplasma gondii cyclic GMP-dependent kinase: chemotherapeutic targeting of an essential parasite protein kinase. Eukaryot. Cell (2002) 1(3):317-328.
   PubMed Web of Science ®Google Scholar
• WATERS NC, GEYER JA: Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development. Expert Opin. Ther. Targets (2003) 7(1):7-17.
   PubMed Web of Science ®Google Scholar
• HOLTON S, MERCKX A, BURGESS D et al.: Structures of P. falciparum PfPK5 test the CDK regulation paradigm and suggest mechanisms of small molecule inhibition. Structure (Camb) (2003) 11(11):1329-1337.
   PubMedGoogle Scholar
• KRISSINEL E, HENRICK K: Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. (2004) 60(Pt. 12 Pt. 1):2256-2268.
   PubMed Web of Science ®Google Scholar
• ZHOU T, RAMAN M, GAO Y et al.: Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K. Structure (2004) 12(10):1891-1900.
   PubMedGoogle Scholar
• KLINKERT MQ, HEUSSLER V: The use of anticancer drugs in antiparasitic chemotherapy. Mini-Rev. Med. Chem. (2006) 6(2):131-143.
   PubMed Web of Science ®Google Scholar
• VAN DE SAND C, HORSTMANN S, SCHMIDT A et al.: The liver stage of Plasmodium berghei inhibits host cell apoptosis. Mol. Microbiol. (2005) 58(3):731-742.
   PubMed Web of Science ®Google Scholar
• PASINI EM, KIRKEGAARD M, MORTENSEN P et al.: In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood (2006) 108(3):791-801.
   PubMed Web of Science ®Google Scholar
• BARVITENKO NN, ADRAGNA NC, WEBER RE: Erythrocyte signal transduction pathways, their oxygenation dependence and functional significance. Cell Physiol. Biochem. (2005) 15(1-4):1-18.
   PubMedGoogle Scholar
• DEL CARLO B, PELLEGRINI M, PELLEGRINO M: Modulation of Ca2+-activated K+ channels of human erythrocytes by endogenous protein kinase C. Biochim. Biophys. Acta (2003) 1612(1):107-116.
   PubMedGoogle Scholar
• MACCAGLIA A, MALLOZZI C, MINETTI M: Differential effects of quercetin and resveratrol on band 3 tyrosine phosphorylation signalling of red blood cells. Biochem. Biophys. Res. Commun. (2003) 305(3):541-547.
   PubMed Web of Science ®Google Scholar
• MANNO S, TAKAKUWA Y, MOHANDAS N: Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation. J. Biol. Chem. (2005) 280(9):7581-7587.
   PubMed Web of Science ®Google Scholar
• HALL BS, DARAMOLA OO, BARDEN G, TARGETT GA: Modulation of protein kinase C activity in Plasmodium falciparum-infected erythrocytes. Blood (1997) 89(5):1770-1778.
   PubMedGoogle Scholar
• MISHRA NC, SHARMA M, SHARMA A: Inhibitory effect of piceatannol, a protein tyrosine kinase inhibitor, on asexual maturation of Plasmodium falciparum. Indian J. Exp. Biol. (1999) 37(4):418-420.
   PubMedGoogle Scholar
• SHARMA A, MISHRA NC: Inhibition of a protein tyrosine kinase activity in Plasmodium falciparum by chloroquine. Indian J. Biochem. Biophys. (1999) 36(5):299-304.
   PubMedGoogle Scholar
• SARTORI M, CEOLOTTO G, SEMPLICINI A: MAPKinase and regulation of the sodium-proton exchanger in human red blood cell. Biochim. Biophys. Acta (1999) 1421(1):140-148.
   PubMedGoogle Scholar
• ZHU J, KRISHNEGOWDA G, GOWDA DC: Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: the requirement of extracellular signal-regulated kinase, p38, c-Jun N-terminal kinase and NF-κB pathways for the expression of proinflammatory cytokines and nitric oxide. J. Biol. Chem. (2005) 280(9):8617-8627.
   PubMed Web of Science ®Google Scholar
• LU Z, SERGHIDES L, PATEL SN et al.: Disruption of JNK2 decreases the cytokine response to Plasmodium falciparum glycosylphosphatidylinositol in vitro and confers protection in a cerebral malaria model. J. Immunol. (2006) 177(9):6344-6352.
   PubMed Web of Science ®Google Scholar
• BERTHET C, ALEEM E, COPPOLA V, TESSAROLLO L, KALDIS P: Cdk2 knockout mice are viable. Curr. Biol. (2003) 13(20):1775-1785.
   PubMed Web of Science ®Google Scholar
• MEIJER L, BORGNE A, MULNER O et al.: Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5. Eur. J. Biochem. (1997) 243(1-2):527-536.
   PubMedGoogle Scholar
• WIRTH DF: Biological revelations. Nature (2002) 419(6906):495-496.
   PubMed Web of Science ®Google Scholar